9HYL
Crystal structure of Trypanosoma brucei trypanothione reductase (TbTR) bound to PROTAC-3
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-06-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.99187 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 101.321, 63.607, 169.271 |
| Unit cell angles | 90.00, 98.23, 90.00 |
Refinement procedure
| Resolution | 46.290 - 2.080 |
| R-factor | 0.18067 |
| Rwork | 0.178 |
| R-free | 0.22400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.566 |
| Data reduction software | autoPROC |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.300 | 2.200 |
| High resolution limit [Å] | 2.080 | 2.080 |
| Number of reflections | 126570 | 40732 |
| <I/σ(I)> | 8.71 | 1.89 |
| Completeness [%] | 97.7 | |
| Redundancy | 6.2 | |
| CC(1/2) | 0.996 | 0.821 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 13-15% PEG3350, 22-24% MPD, 40 mM imidazole pH 8.0, 50 mM NaBr |
